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collagen proline hydroxylase
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egg-laying abnormal-9 prolyl hydroxylase
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EGLN prolyl hydroxylase
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HIF prolyl-4-hydroxylase
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hydroxylase, collagen proline
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hypoxia inducible factor prolyl-4-hydroxylase domain-containing protein
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peptidyl proline hydroxylase
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procollagen prolyl 4-hydroxylase
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procollagen-proline dioxygenase
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proline hydroxylase
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proline protocollagen hydroxylase
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proline, 2-oxoglutarate dioxygenase
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proline,2-oxoglutarate 4-dioxygenase
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prolyl-4-hydroxylase alpha I
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prolyl-4-hydroxylase alpha II
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prolyl-4-hydroxylase alpha1
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prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase, 4-hydroxylating
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prolylprotocollagen dioxygenase
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prolylprotocollagen hydroxylase
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protocollagen hydroxylase
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protocollagen proline 4-hydroxylase
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protocollagen proline dioxygenase
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protocollagen proline hydroxylase
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protocollagen prolyl hydroxylase
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type I proly 4-hydroxylase
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additional information
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the enzyme belongs to the P4H enzyme family of the 2-oxoglutarate-dependent dioxygenases
prolyl 4-hydroxylase
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prolyl hydroxylase
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procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
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(Gly-Ala-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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active substrate
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?
(Gly-Pro-Ala)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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poor substrate
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?
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
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r
(Pro-Gly-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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active substrate
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?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
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n: 1,5,10
n: 1,5,10
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hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia inducible factor trans-4-hydroxy-L-proline + succinate + CO2
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hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
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?
additional information
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hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
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i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunti is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview
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hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
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i.e. HIF
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?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
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?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
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?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
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?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
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procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
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proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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additional information
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additional information
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thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
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additional information
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substrate and ligand binding structures, overview
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additional information
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the BH4 domain is required for the interaction of PHD3 with Bcl-2, PHD3 promotes apoptosis via its BH4 domain
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1,4-dihydrophenanthroline-4-one-3-carboxylic acid
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potent competitive inhibitor of collagen hydroxylation in the oestradiol-stimulated uterus in vivo
8-(N-butyl-N-ethylcarbamoyl)-1,4-dihydrophenanthrolin-4-one-3-carboxylic acid
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potent competitive inhibitor of collagen hydroxylation in the oestradiol-stimulated uterus in vivo
8-hydroxyquinoline
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inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
alpha,alpha'-dipyridyl
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an Fe2+ chelator
antimycin A
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18% inhibition at 0.02 mM
Cd2+
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competitive versus Fe2+
ciclopirox olamine
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an Fe2+ chelator
Co2+
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competitive versus Fe2+
Cupferron
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28% inhibition at 0.02 mM
diethyldithiocarbamate
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10% inhibition at 0.02 mM
Diethylenetriaminepentaacetic acid
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inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
dimethyl oxalylglycine
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DMOG, the effect is HIF-independent
dithiothreitol
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powerful inhibitor at 1 mM
gelatin
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commercial, inhibitor
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HOE077
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decrease in enzyme activity by 15%
Ketomalonate
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100% inhibition at 1 mM, acts by chelating ferrous ion rather than by competing with alpha-ketoglutarate
L-mimosine
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50 mg/kg/day for 2 weeks
malonate
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19% inhibition at 1 mM
N-Hydroxyethylenediaminetriacetic acid
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inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
Ni2+
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competitive versus Fe2+
oxalate
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34% inhibition at 1 mM
propyl gallate
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100% inhibition at 2 mM
rosiglitazone
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decrease in enzyme activity by 32.3%
succinate
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51% inhibition at 1 mM
trifluorothienylbutanedione
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48% inhibition at 0.05 mM
Zn2+
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competitive versus Fe2+
additional information
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hypoxia inhibits the enzyme
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1,10-phenanthroline
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inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
1,10-phenanthroline
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91% inhibition at 0.02 mM
2,2'-dipyridyl
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inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
2,2'-dipyridyl
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87% inhibition at 0.02 mM
desferrioxamine
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desferrioxamine
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an Fe2+ chelator
EDTA
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inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
EDTA
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64% inhibition at 0.02 mM
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metabolism
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pharmacologic inactivation of EGLN3 hydroxylase results in activation of the canonical NF-kappaB pathway
physiological function
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4-hydroxylation of proline is essential for the thermal stability of collagen triple helices, non-hydroxylated collagen polypeptide chains cannot form functional molecules in vivo. The enzyme also acts as hypoxia-inducible transcription factor, HIF, and occurs in three different isozyme forms
physiological function
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egg-laying abnormal-9 prolyl hydroxylases regulate the stability and thereby the activity of the alpha-subunits of hypoxia-inducible factor through its ability to catalyze their hydroxylation. EGLN3 promotes differentiation of C2C12 skeletal myoblasts. EGLN3 is a negative regulator of NF-kappaB, and its prolyl hydroxylase activity is required for this effect. EGLN3 is involved in mediating myogenic differentiation, which is HIF-independent
physiological function
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role of PHD3 in the apoptosis of cardiac myocytes. PHD3 promotes the apoptosis of H9c2 cells via an interaction with the BH4 domain of Bcl-2, it affects the formation of the Bax-Bcl-2 complex
physiological function
prolyl-4-hydroxylase alpha1 and matrix metalloproteinases are essential for collagen synthesis and degradation. The enzyme is induced by mechanical stretch on the vessel wall, an important stimulus that also induces collagen remodeling, mechanical stretch increases MMP-2 andP4H alpha1 expression in human aortic smooth muscle cell via AKT-P38 MAPK-JNK signaling, thereby inducing vascular remodeling. .. MMP-2 and P4Halpha1 participate in collagen metabolism induced by pathologic mechanical stretch
additional information
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exogenous expression of wild-type EGLN3, but not of its catalytically inactive mutant, significantly inhibits NF-kappaB activation induced by overexpressed TRAF2 or IkappaB kinase 2, overview. Deletion of EGLN3 by small interfering RNAs leads to activation of NF-kappaB
additional information
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PHD3 upregulation contributes to doxorubicin-induced apoptosis in H9c2 cells. Overexpression of PHD3 counteracts the formation of the Bax-Bcl-2 complex, the BH4 domain of anti-apoptosis protein Bcl-2 is required for its interaction with PHD3. Bax-Bcl-2 complex formation is significantly reduced in apoptotic H9c2 cells in which PHD3 is overexpressed compared to the apoptotic H9c2 cells with native PHD3 levels
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Kivirikko, K.I.; Myllyl, R.
The hydroxylation of prolyl and lysyl residues
Enzymol. Post- transl. Modif. Proteins (Freedman, R. B. , Hawkins, H. C. , eds. ) Academic Press, New York
1
53-104
1980
Gallus gallus, Homo sapiens, Rattus norvegicus
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brenda
Kivirikko, K.I.; Myllyl, R.
Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes
Methods Enzymol.
82
245-304
1982
Gallus gallus, Homo sapiens, Rattus norvegicus
brenda
Takeda, K.; Katoh, F.; Kawai, S.; Konno, K.
Stimulation of prolyl hydroxylase activity by chelating agents
Arch. Biochem. Biophys.
197
273-276
1979
Rattus norvegicus
brenda
Tryggvason, K.; Majamaa, K.; Kivirikko, K.I.
Prolyl 3-hydroxylase and 4-hydroxylase activities in certain rat and chick-embryo tissues and age-related changes in their activities in the rat
Biochem. J.
178
127-131
1979
Gallus gallus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Tryggvason, K.; Risteli, J.; Kivirikko, K.I.
Separation of prolyl 3-hydroxylase and 4-hydroxylase activities and the 4-hydroxyproline requirement for synthesis of 3-hydroxyproline
Biochem. Biophys. Res. Commun.
76
275-281
1977
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Risteli, J.; Tuderman, L.; Kivirikko, K.I.
Intracellular enzymes of collagen biosynthesis in rat liver as a function of age and in hepatic injury induced by dimethylnitrosamine. Purification of rat prolyl hydroxylase and comparison of changes in prolyl hydroxylase activity with changes in immunoreactive prolyl hydroxylase
Biochem. J.
158
369-376
1976
Rattus norvegicus
brenda
Adams, E.; Lamon, M.
Prolyl hydroxylase of earthworms. Substrate specificity of an enzyme from the subcuticular epithelium
J. Biol. Chem.
252
7591-7597
1977
Lumbricus terrestris, Rattus norvegicus
brenda
Hutton, J.J.; Tappel, A.L.; Udenfried, S.
Cofactor and substrate requirements of collagen proline hydroxylase
Arch. Biochem. Biophys.
118
231-240
1967
Cavia porcellus, Gallus gallus, Rattus norvegicus
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brenda
Franklin, T.J.; Morris, W.P.; Edwards, P.N.; Large, M.S.; Stephenson, R.
Inhibition of prolyl 4-hydroxylase in vitro and in vivo by members of a novel series of phenanthrolinones
Biochem. J.
353
333-338
2001
Gallus gallus, Homo sapiens, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Nissi, R.; Bohling, T.; Autio-Harmainen, H.
Immunofluorescence localization of prolyl 4-hydroxylase isoenzymes and type I and II collagens in bone tumours: type I enzyme predominates in osteosarcomas and chondrosarcomas, whereas type II enzyme predominates in their benign counterparts
Acta Histochem.
106
111-121
2004
Homo sapiens, Rattus norvegicus
brenda
Hofbauer, K.h.; Gess, B.; Lohaus, C.; Meyer, H.E.; Katschinski, D.; Kurtz, A.
Oxygen tension regulates the expression of a group of procollagen hydroxylases
Eur. J. Biochem.
270
4515-4522
2003
Rattus norvegicus, Rattus norvegicus (P54001)
brenda
Kukkola, L.; Hieta, R.; Kivirikko, K.I.; Myllyharju, J.
Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme
J. Biol. Chem.
278
47685-47693
2003
Rattus norvegicus (Q6W3E9), Mus musculus (Q6W3F0), Mus musculus, Homo sapiens (Q7Z4N8), Homo sapiens
brenda
Li, N.; Yi, F.; Sundy, C.M.; Chen, L.; Hilliker, M.L.; Donley, D.K.; Muldoon, D.B.; Li, P.L.
Expression and actions of HIF prolyl-4-hydroxylase in the rat kidneys
Am. J. Physiol. Renal Physiol.
292
F207-F216
2007
Rattus norvegicus
brenda
Choi, H.J.; Soh, Y.
An assay method for screening inhibitors of prolyl 4-hydroxylase in immortalized rat hepatic stellate HSC-T6 cells
J. Appl. Pharmacol.
15
261-265
2007
Rattus norvegicus
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brenda
Myllyharju, J.
Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets
Ann. Med.
40
402-417
2008
Caenorhabditis elegans, Chlamydomonas reinhardtii, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Liu, Y.; Huo, Z.; Yan, B.; Lin, X.; Zhou, Z.N.; Liang, X.; Zhu, W.; Liang, D.; Li, L.; Liu, Y.; Zhao, H.; Sun, Y.; Chen, Y.H.
Prolyl hydroxylase 3 interacts with Bcl-2 to regulate doxorubicin-induced apoptosis in H9c2 cells
Biochem. Biophys. Res. Commun.
401
231-237
2010
Rattus norvegicus
brenda
Fu, J.; Taubman, M.B.
Prolyl hydroxylase EGLN3 regulates skeletal myoblast differentiation through an NF-kappaB-dependent pathway
J. Biol. Chem.
285
8927-8935
2010
Rattus norvegicus
brenda
Liu, X.; Huang, X.; Chen, L.; Zhang, Y.; Li, M.; Wang, L.; Ge, C.; Wang, H.; Zhang, M.
Mechanical stretch promotes matrix metalloproteinase-2 and prolyl-4-hydroxylase alpha1 production in human aortic smooth muscle cells via Akt-p38 MAPK-JNK signaling
Int. J. Biochem. Cell Biol.
62
15-23
2015
Homo sapiens (P13674), Homo sapiens, Rattus norvegicus (P54001), Rattus norvegicus Wistar (P54001)
brenda